PMID- 12423314
OWN - NLM
STAT- MEDLINE
DCOM- 20021213
LR  - 20190513
IS  - 0019-2805 (Print)
IS  - 1365-2567 (Electronic)
IS  - 0019-2805 (Linking)
VI  - 107
IP  - 3
DP  - 2002 Nov
TI  - Necessity of the stalk region for immunoglobulin E interaction with CD23.
PG  - 373-81
AB  - Previously, a soluble mouse CD23 chimera, composed of an N-terminal trimeric 
      isoleucine zipper motif (lz) followed by the entire extracellular region (amino 
      acids 48-331) of CD23 (lz-CD2348-331), was prepared and exhibited strong binding 
      to rodent immunoglobulin E (IgE). In the current study, we report the 
      construction of a similar human chimeric protein (lz-huCD2345-321), as well as a 
      series of murine chimeric lz-CD23 mutants with incremental portions of stalk 
      deleted, to further investigate the role of the stalk region in mediating the 
      CD23-IgE interaction. All chimeric proteins were designed such that the predicted 
      heptad structure of the stalk was retained. IgE binding, as determined by the 
      capacity to inhibit 125I-IgE from binding to FcepsilonRI-bearing RBL-2H3 cells, 
      and by surface plasmon-resonance analysis using an IgE-coated sensor chip, was 
      unchanged from the original lz chimera and the binding parameters were similar to 
      those of cell-surface CD23. The minimal murine chimera that retained IgE-binding 
      activity was lz-CD23139-331, which still contains 35 amino acids of the stalk 
      region. When the lz motif was linked to CD23 amino acid 157 (or higher), 
      significant IgE-binding capacity was lost. With human lz-CD23, as with mouse, 
      deletion of the stalk greatly reduced IgE-binding ability. In summary, the data 
      support the concept that at least a portion of the stalk region of CD23 plays a 
      crucial role in maintaining high-affinity/avidity interaction with IgE. The 
      lz-CD23 constructs represent a possible alternative for both blocking the 
      IgE/FcepsilonRI interaction and inhibiting IgE production by B lymphocytes.
FAU - Chen, Bing-Hung
AU  - Chen BH
AD  - Department of Microbiology and Immunology, Virginia Commonwealth University, 
      Richmond, VA 23298, USA.
FAU - Ma, Check
AU  - Ma C
FAU - Caven, Timothy H
AU  - Caven TH
FAU - Chan-Li, Yee
AU  - Chan-Li Y
FAU - Beavil, Andrew
AU  - Beavil A
FAU - Beavil, Rebecca
AU  - Beavil R
FAU - Gould, Hannah
AU  - Gould H
FAU - Conrad, Daniel H
AU  - Conrad DH
LA  - eng
GR  - R01 AI018697/AI/NIAID NIH HHS/United States
GR  - AI 44163/AI/NIAID NIH HHS/United States
GR  - R01 AI044163/AI/NIAID NIH HHS/United States
GR  - AI 18697/AI/NIAID NIH HHS/United States
GR  - T32 AI 07047/AI/NIAID NIH HHS/United States
GR  - T32 AI007047/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Immunology
JT  - Immunology
JID - 0374672
RN  - 0 (Receptors, IgE)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 37341-29-0 (Immunoglobulin E)
SB  - IM
MH  - Animals
MH  - Antibody Affinity
MH  - Binding, Competitive
MH  - Humans
MH  - Immunoglobulin E/*metabolism
MH  - Mutagenesis, Site-Directed
MH  - Protein Binding
MH  - Rats
MH  - Receptors, IgE/genetics/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Structure-Activity Relationship
MH  - Surface Plasmon Resonance
MH  - Tumor Cells, Cultured
PMC - PMC1782806
EDAT- 2002/11/09 04:00
MHDA- 2002/12/17 04:00
PMCR- 2003/11/01
CRDT- 2002/11/09 04:00
PHST- 2002/11/09 04:00 [pubmed]
PHST- 2002/12/17 04:00 [medline]
PHST- 2002/11/09 04:00 [entrez]
PHST- 2003/11/01 00:00 [pmc-release]
AID - 1512 [pii]
AID - 10.1046/j.1365-2567.2002.01512.x [doi]
PST - ppublish
SO  - Immunology. 2002 Nov;107(3):373-81. doi: 10.1046/j.1365-2567.2002.01512.x.